NEW INSIGHTS INTO THE PATHOGENESIS OF HEMODIALYSIS-ASSOCIATED AMYLOIDOSIS

[21] Husebekk A, Skogen B, Husby G, Marhaug G, Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo, Scand J Immunol, 21, pp. 283-287, (1985)

[22] Saraiva MJM, Birken S, Costa PP, Goodman DS, Family studies of the genetic abnormality in transthyretin (prealbumin) in Portuguese patients with familial amyloidotic neuropathy, Annals of the New York Academy of Sciences, 435, pp. 86-100, (1984)

[23] Nakazato M, Kangawa K, Minamino N, Tawara S, Matsuo H, Araki S, Revised analysis of amino acid replacement in a prealbumin variant (SKO‐III) associated with familial amyloidotic polyneuropathy of Jewish origin, Biochim Biophys Res Commun, 123, pp. 921-928, (1984)

[24] Wallace MR, Dwulet FE, Conneally PM, Benson MD, Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis, J Clin Invest, 78, pp. 6-12, (1986)

[25] Dwulet FE, Benson MD, Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss), J Clin Invest, 78, pp. 880-886, (1986)

[26] Ericson LH, Eriksen N, Walsh KA, Benditt EP, Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor, FEBS Letters, 218, pp. 11-16, (1987)

[27] Buxbaum J, Aberrant immunoglobulin synthesis in light chain amyloidosis, J Clin Invest, 78, pp. 798-806, (1986)

[28] Werdelin O, Ranlov P, Amyloidosis in mice produced by transplantation of spleen cells from casein‐treated mice, Acta Pathol Microbiol Immunol Scand, 68, pp. 1-8, (1966)

[29] Kisilevsky R, Boudreau L, Kinetics of amyloid deposition. I. The effects of amyloid enhancing factor and splenectomy, Lab Invest, 48, pp. 53-59, (1983)

[30] Snow AD, Willmer J, Kisilevsky R, Sulfated glycosaminoglycans: A common constituent of all amyloids, Lab Invest, 56, pp. 120-123, (1987)

[21] Husebekk A, Skogen B, Husby G, Marhaug G, Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo, Scand J Immunol, 21, pp. 283-287, (1985)

[22] Saraiva MJM, Birken S, Costa PP, Goodman DS, Family studies of the genetic abnormality in transthyretin (prealbumin) in Portuguese patients with familial amyloidotic neuropathy, Annals of the New York Academy of Sciences, 435, pp. 86-100, (1984)

[23] Nakazato M, Kangawa K, Minamino N, Tawara S, Matsuo H, Araki S, Revised analysis of amino acid replacement in a prealbumin variant (SKO‐III) associated with familial amyloidotic polyneuropathy of Jewish origin, Biochim Biophys Res Commun, 123, pp. 921-928, (1984)

[24] Wallace MR, Dwulet FE, Conneally PM, Benson MD, Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis, J Clin Invest, 78, pp. 6-12, (1986)

[25] Dwulet FE, Benson MD, Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss), J Clin Invest, 78, pp. 880-886, (1986)

[26] Ericson LH, Eriksen N, Walsh KA, Benditt EP, Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor, FEBS Letters, 218, pp. 11-16, (1987)

[27] Buxbaum J, Aberrant immunoglobulin synthesis in light chain amyloidosis, J Clin Invest, 78, pp. 798-806, (1986)

[28] Werdelin O, Ranlov P, Amyloidosis in mice produced by transplantation of spleen cells from casein‐treated mice, Acta Pathol Microbiol Immunol Scand, 68, pp. 1-8, (1966)

[29] Kisilevsky R, Boudreau L, Kinetics of amyloid deposition. I. The effects of amyloid enhancing factor and splenectomy, Lab Invest, 48, pp. 53-59, (1983)

[30] Snow AD, Willmer J, Kisilevsky R, Sulfated glycosaminoglycans: A common constituent of all amyloids, Lab Invest, 56, pp. 120-123, (1987)